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Article ; Online: The origin story of rapamycin: systemic bias in biomedical research and cold war politics.

Powers, Ted

2022 Volume 33, Issue 13, Page(s) pe7

Abstract: METEI (Medical Expedition to Easter Island) was a Canadian-led expedition to Easter Island in 1964 that led to the discovery of rapamycin, launching a billion-dollar drug industry and major field of biomedical research. ...

Abstract	METEI (Medical Expedition to Easter Island) was a Canadian-led expedition to Easter Island in 1964 that led to the discovery of rapamycin, launching a billion-dollar drug industry and major field of biomedical research.
MeSH term(s)	Biomedical Research ; Canada ; Pharmaceutical Preparations ; Politics ; Sirolimus/pharmacology
Chemical Substances	Pharmaceutical Preparations ; Sirolimus (W36ZG6FT64)
Language	English
Publishing date	2022-10-13
Publishing country	United States
Document type	Journal Article
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E22-08-0377
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Zs.A 2853: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Identification of defined structural elements within TOR2 kinase required for TOR complex 2 assembly and function in

Tsverov, Jennifer / Yegorov, Kristina / Powers, Ted

Molecular biology of the cell

2022 Volume 33, Issue 5, Page(s) ar44

Abstract: The mammalian target of rapamycin (mTOR) is a large protein kinase that assembles into two multisubunit protein complexes, mTORC1 and mTORC2, to regulate cell growth in eukaryotic cells. While significant progress has been made in our understanding of ... ...

Abstract	The mammalian target of rapamycin (mTOR) is a large protein kinase that assembles into two multisubunit protein complexes, mTORC1 and mTORC2, to regulate cell growth in eukaryotic cells. While significant progress has been made in our understanding of the composition and structure of these complexes, important questions remain regarding the role of specific sequences within mTOR important for complex formation and activity. To address these issues, we have used a molecular genetic approach to explore TOR complex assembly in budding yeast, where two closely related TOR paralogues, TOR1 and TOR2, partition preferentially into TORC1 versus TORC2, respectively. We previously identified an ∼500-amino-acid segment within the N-terminal half of each protein, termed the major assembly specificity (MAS) domain, which can govern specificity in formation of each complex. In this study, we have extended the use of chimeric TOR1-TOR2 genes as a "sensitized" genetic system to identify specific subdomains rendered essential for TORC2 function, using synthetic lethal interaction analyses. Our findings reveal important design principles underlying the dimeric assembly of TORC2 as well as identifying specific segments within the MAS domain critical for TORC2 function, to a level approaching single-amino-acid resolution. Together these findings highlight the complex and cooperative nature of TOR complex assembly and function.
MeSH term(s)	Cell Cycle Proteins/metabolism ; Mechanistic Target of Rapamycin Complex 1/metabolism ; Mechanistic Target of Rapamycin Complex 2/metabolism ; Phosphatidylinositol 3-Kinases/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Cell Cycle Proteins ; Saccharomyces cerevisiae Proteins ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Mechanistic Target of Rapamycin Complex 2 (EC 2.7.11.1)
Language	English
Publishing date	2022-03-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E21-12-0611
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Article ; Online: Target of rapamycin signaling mediates vacuolar fragmentation.

Stauffer, Bobbiejane / Powers, Ted

Current genetics

2017 Volume 63, Issue 1, Page(s) 35–42

Abstract: In eukaryotic cells, cellular homeostasis requires that different organelles respond to intracellular as well as environmental signals and modulate their behavior as conditions demand. Understanding the molecular mechanisms required for these changes ... ...

Abstract	In eukaryotic cells, cellular homeostasis requires that different organelles respond to intracellular as well as environmental signals and modulate their behavior as conditions demand. Understanding the molecular mechanisms required for these changes remains an outstanding goal. One such organelle is the lysosome/vacuole, which undergoes alterations in size and number in response to environmental and physiological stimuli. Changes in the morphology of this organelle are mediated in part by the equilibrium between fusion and fission processes. While the fusion of the yeast vacuole has been studied intensively, the regulation of vacuolar fission remains poorly characterized by comparison. In recent years, a number of studies have incorporated genome-wide visual screens and high-throughput microscopy to identify factors required for vacuolar fission in response to diverse cellular insults, including hyperosmotic and endoplasmic reticulum stress. Available evidence now demonstrates that the rapamycin-sensitive TOR network, a master regulator of cell growth, is required for vacuolar fragmentation in response to stress. Importantly, many of the genes identified in these studies provide new insights into potential links between the vacuolar fission machinery and TOR signaling. Together these advances both extend our understanding of the regulation of vacuolar fragmentation in yeast as well as underscore the role of analogous events in mammalian cells.
MeSH term(s)	Animals ; Biological Transport ; Gene Expression Regulation ; Humans ; Intracellular Membranes/metabolism ; Mechanistic Target of Rapamycin Complex 1 ; Multiprotein Complexes/metabolism ; Protein Binding ; Protein Transport ; Signal Transduction ; Stress, Physiological ; TOR Serine-Threonine Kinases/metabolism ; Vacuoles/metabolism ; Yeasts/genetics ; Yeasts/metabolism
Chemical Substances	Multiprotein Complexes ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1)
Language	English
Publishing date	2017-02
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	282876-5
ISSN	1432-0983 ; 0172-8083
ISSN (online)	1432-0983
ISSN	0172-8083
DOI	10.1007/s00294-016-0616-0
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Zs.A 2586: Show issues

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Article ; Online: Cell growth control: mTOR takes on fat.

Powers, Ted

Molecular cell

2008 Volume 31, Issue 6, Page(s) 775–776

Abstract: In a recent issue of Cell Metabolism, Porstmann et al. (2008) demonstrate that fatty acid biosynthesis, under the transcriptional control of SREBP1, is regulated by the rapamycin-sensitive mTOR signaling network, thus expanding the scope of biosynthetic ... ...

Abstract	In a recent issue of Cell Metabolism, Porstmann et al. (2008) demonstrate that fatty acid biosynthesis, under the transcriptional control of SREBP1, is regulated by the rapamycin-sensitive mTOR signaling network, thus expanding the scope of biosynthetic processes integrated by mTOR.
MeSH term(s)	Animals ; Cell Proliferation ; Cholesterol/metabolism ; Fatty Acids/metabolism ; Humans ; Mice ; Protein Kinases/metabolism ; Sterol Regulatory Element Binding Proteins/metabolism ; TOR Serine-Threonine Kinases ; Transcription Factors/metabolism
Chemical Substances	Fatty Acids ; Sterol Regulatory Element Binding Proteins ; Transcription Factors ; Cholesterol (97C5T2UQ7J) ; Protein Kinases (EC 2.7.-) ; MTOR protein, human (EC 2.7.1.1) ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; mTOR protein, mouse (EC 2.7.1.1)
Language	English
Publishing date	2008-09-26
Publishing country	United States
Document type	Comment ; Journal Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2008.09.006
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Article ; Online: Redesigning TOR Kinase to Explore the Structural Basis for TORC1 and TORC2 Assembly.

Hill, Andrew / Niles, Brad / Cuyegkeng, Andrew / Powers, Ted

Biomolecules

2018 Volume 8, Issue 2

Abstract: TOR is a serine/threonine protein kinase that assembles into distinct TOR Complexes 1 and 2 (TORC1 or TORC2) to regulate cell growth. In mammalian cells, a single mTOR incorporates stably into mTORC1 and mTORC2. By contrast, ... ...

Abstract	TOR is a serine/threonine protein kinase that assembles into distinct TOR Complexes 1 and 2 (TORC1 or TORC2) to regulate cell growth. In mammalian cells, a single mTOR incorporates stably into mTORC1 and mTORC2. By contrast, in
MeSH term(s)	Cell Cycle Proteins/chemistry ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Mechanistic Target of Rapamycin Complex 1/metabolism ; Mechanistic Target of Rapamycin Complex 2/metabolism ; Phosphatidylinositol 3-Kinases/chemistry ; Phosphatidylinositol 3-Kinases/genetics ; Phosphatidylinositol 3-Kinases/metabolism ; Protein Binding ; Protein Domains ; Protein Multimerization ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Cell Cycle Proteins ; Saccharomyces cerevisiae Proteins ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; TOR1 protein, S cerevisiae (EC 2.7.1.137) ; TOR2 protein, S cerevisiae (EC 2.7.1.137) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Mechanistic Target of Rapamycin Complex 2 (EC 2.7.11.1)
Language	English
Publishing date	2018-06-01
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom8020036
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Article: TOR signaling and S6 kinase 1: Yeast catches up.

Powers, Ted

Cell metabolism

2007 Volume 6, Issue 1, Page(s) 1–2

Abstract: Conservation of the rapamycin-sensitive TOR signaling network among eukaryotes has been instrumental to the rapid progress made in this field in recent years. A recent report in Molecular Cell (Urban et al., 2007) now extends this conservation to include ...

Abstract	Conservation of the rapamycin-sensitive TOR signaling network among eukaryotes has been instrumental to the rapid progress made in this field in recent years. A recent report in Molecular Cell (Urban et al., 2007) now extends this conservation to include Sch9, an AGC protein kinase family member from S. cerevisiae, which appears to be the long sought after yeast ortholog of mammalian S6 kinase 1 (S6K1) and a direct target for the rapamycin-sensitive TOR complex I.
MeSH term(s)	Animals ; Cell Division/physiology ; Humans ; Protein Kinases/metabolism ; Ribosomal Protein S6 Kinases/metabolism ; Saccharomyces cerevisiae/physiology ; Signal Transduction ; TOR Serine-Threonine Kinases
Chemical Substances	Protein Kinases (EC 2.7.-) ; MTOR protein, human (EC 2.7.1.1) ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; Ribosomal Protein S6 Kinases (EC 2.7.11.1)
Language	English
Publishing date	2007-07
Publishing country	United States
Document type	Comment ; Journal Article ; Review
ZDB-ID	2176834-1
ISSN	1932-7420 ; 1550-4131
ISSN (online)	1932-7420
ISSN	1550-4131
DOI	10.1016/j.cmet.2007.06.009
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Article ; Online: Target of rapamycin signaling mediates vacuolar fission caused by endoplasmic reticulum stress in Saccharomyces cerevisiae.

Stauffer, Bobbiejane / Powers, Ted

Molecular biology of the cell

2015 Volume 26, Issue 25, Page(s) 4618–4630

Abstract: The yeast vacuole is equivalent to the mammalian lysosome and, in response to diverse physiological and environmental stimuli, undergoes alterations both in size and number. Here we demonstrate that vacuoles fragment in response to stress within the ... ...

Abstract	The yeast vacuole is equivalent to the mammalian lysosome and, in response to diverse physiological and environmental stimuli, undergoes alterations both in size and number. Here we demonstrate that vacuoles fragment in response to stress within the endoplasmic reticulum (ER) caused by chemical or genetic perturbations. We establish that this response does not involve known signaling pathways linked previously to ER stress but instead requires the rapamycin-sensitive TOR Complex 1 (TORC1), a master regulator of cell growth, together with its downstream effectors, Tap42/Sit4 and Sch9. To identify additional factors required for ER stress-induced vacuolar fragmentation, we conducted a high-throughput, genome-wide visual screen for yeast mutants that are refractory to ER stress-induced changes in vacuolar morphology. We identified several genes shown previously to be required for vacuolar fusion and/or fission, validating the utility of this approach. We also identified a number of new components important for fragmentation, including a set of proteins involved in assembly of the V-ATPase. Remarkably, we find that one of these, Vph2, undergoes a change in intracellular localization in response to ER stress and, moreover, in a manner that requires TORC1 activity. Together these results reveal a new role for TORC1 in the regulation of vacuolar behavior.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Cell Proliferation/genetics ; Endoplasmic Reticulum/genetics ; Endoplasmic Reticulum Stress/genetics ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Signal Transduction ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Vacuoles/genetics ; Vacuoles/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Membrane Proteins ; Molecular Chaperones ; Saccharomyces cerevisiae Proteins ; TAP42 protein, S cerevisiae ; TORC1 protein complex, S cerevisiae ; Transcription Factors ; VPH2 protein, S cerevisiae ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; SCH9 protein, S cerevisiae (EC 2.7.11.1)
Language	English
Publishing date	2015-12-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E15-06-0344
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Article ; Online: TOR complex 2-Ypk1 signaling regulates actin polarization via reactive oxygen species.

Niles, Brad J / Powers, Ted

Molecular biology of the cell

2014 Volume 25, Issue 24, Page(s) 3962–3972

Abstract: The evolutionarily conserved mTOR complex 2 (mTORC2) signaling pathway is an important regulator of actin cytoskeletal architecture and, as such, is a candidate target for preventing cancer cell motility and invasion. Remarkably, the precise mechanism(s) ...

Abstract	The evolutionarily conserved mTOR complex 2 (mTORC2) signaling pathway is an important regulator of actin cytoskeletal architecture and, as such, is a candidate target for preventing cancer cell motility and invasion. Remarkably, the precise mechanism(s) by which mTORC2 regulates the actin cytoskeleton have remained elusive. Here we show that in budding yeast, TORC2 and its downstream kinase Ypk1 regulate actin polarization by controlling reactive oxygen species (ROS) accumulation. Specifically, we find that TORC2-Ypk1 regulates actin polarization both by vacuole-related ROS, controlled by the phospholipid flippase kinase Fpk1 and sphingolipids, and by mitochondria-mediated ROS, controlled by the PKA subunit Tpk3. In addition, we find that the protein kinase C (Pkc1)/MAPK cascade, a well-established regulator of actin, acts downstream of Ypk1 to regulate ROS, in part by promoting degradation of the oxidative stress responsive repressor, cyclin C. Furthermore, we show that Ypk1 regulates Pkc1 activity through proper localization of Rom2 at the plasma membrane, which is also dependent on Fpk1 and sphingolipids. Together these findings demonstrate important links between TORC2/Ypk1 signaling, Fpk1, sphingolipids, Pkc1, and ROS as regulators of actin and suggest that ROS may play an important role in mTORC2-dependent dysregulation of the actin cytoskeleton in cancer cells.
MeSH term(s)	Actin Cytoskeleton/metabolism ; Actins/metabolism ; Blotting, Western ; Cyclin C/genetics ; Cyclin C/metabolism ; Glycogen Synthase Kinase 3/genetics ; Glycogen Synthase Kinase 3/metabolism ; Mechanistic Target of Rapamycin Complex 2 ; Microscopy, Fluorescence ; Mitogen-Activated Protein Kinases/metabolism ; Multiprotein Complexes/metabolism ; Mutation ; Phosphorylation ; Protein Binding ; Protein Kinase C/metabolism ; Protein Kinases/genetics ; Protein Kinases/metabolism ; Protein Subunits/metabolism ; Reactive Oxygen Species/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Signal Transduction ; Sphingolipids/metabolism ; TOR Serine-Threonine Kinases/metabolism
Chemical Substances	Actins ; Cyclin C ; Multiprotein Complexes ; Protein Subunits ; Reactive Oxygen Species ; Saccharomyces cerevisiae Proteins ; Sphingolipids ; Protein Kinases (EC 2.7.-) ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; Fpk1 protein, S cerevisiae (EC 2.7.11.1) ; Mechanistic Target of Rapamycin Complex 2 (EC 2.7.11.1) ; PKC1 protein, S cerevisiae (EC 2.7.11.13) ; Protein Kinase C (EC 2.7.11.13) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Glycogen Synthase Kinase 3 (EC 2.7.11.26) ; MCK1 protein, S cerevisiae (EC 2.7.12.1)
Language	English
Publishing date	2014-09-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E14-06-1122
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Article ; Online: A role for TOR complex 2 signaling in promoting autophagy.

Vlahakis, Ariadne / Powers, Ted

Autophagy

2014 Volume 10, Issue 11, Page(s) 2085–2086

Abstract: The conserved target of rapamycin (TOR) kinase is a central regulator of cell growth in response to nutrient availability. TOR forms 2 structurally and functionally distinct complexes, TORC1 and TORC2, and negatively regulates autophagy via TORC1. Here ... ...

Abstract	The conserved target of rapamycin (TOR) kinase is a central regulator of cell growth in response to nutrient availability. TOR forms 2 structurally and functionally distinct complexes, TORC1 and TORC2, and negatively regulates autophagy via TORC1. Here we demonstrate TOR also operates independently through the TORC2 signaling pathway to promote autophagy upon amino acid limitation. Under these conditions, TORC2, through its downstream target kinase Ypk1, inhibits the Ca(2+)- and Cmd1/calmodulin-dependent phosphatase, calcineurin, to enable the activation of the amino acid-sensing EIF2S1/eIF2α kinase, Gcn2, and promote autophagy. Thus TORC2 signaling regulates autophagy in a pathway distinct from TORC1 to provide a tunable response to the cellular metabolic state.
MeSH term(s)	Amino Acids/chemistry ; Autophagy ; Calcineurin/metabolism ; Calcium/chemistry ; Calcium/metabolism ; Disease Progression ; Glycogen Synthase Kinase 3/metabolism ; Mechanistic Target of Rapamycin Complex 1 ; Mechanistic Target of Rapamycin Complex 2 ; Multiprotein Complexes/metabolism ; Nitrogen/chemistry ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Signal Transduction ; TOR Serine-Threonine Kinases/metabolism
Chemical Substances	Amino Acids ; Multiprotein Complexes ; Saccharomyces cerevisiae Proteins ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Mechanistic Target of Rapamycin Complex 2 (EC 2.7.11.1) ; Glycogen Synthase Kinase 3 (EC 2.7.11.26) ; MCK1 protein, S cerevisiae (EC 2.7.12.1) ; Calcineurin (EC 3.1.3.16) ; Nitrogen (N762921K75) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2014
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.4161/auto.36262
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Article ; Online: Stress-response transcription factors Msn2 and Msn4 couple TORC2-Ypk1 signaling and mitochondrial respiration to ATG8 gene expression and autophagy.

Vlahakis, Ariadne / Lopez Muniozguren, Nerea / Powers, Ted

Autophagy

2017 Volume 13, Issue 11, Page(s) 1804–1812

Abstract: Macroautophagy/autophagy is a starvation and stress-induced catabolic process critical for cellular homeostasis and adaptation. Several Atg proteins are involved in the formation of the autophagosome and subsequent degradation of cytoplasmic components, ... ...

Abstract	Macroautophagy/autophagy is a starvation and stress-induced catabolic process critical for cellular homeostasis and adaptation. Several Atg proteins are involved in the formation of the autophagosome and subsequent degradation of cytoplasmic components, a process termed autophagy flux. Additionally, the expression of several Atg proteins, in particular Atg8, is modulated transcriptionally, yet the regulatory mechanisms involved remain poorly understood. Here we demonstrate that the AGC kinase Ypk1, target of the rapamycin-insensitive TORC2 signaling pathway, controls ATG8 expression by repressing the heterodimeric Zinc-finger transcription factors Msn2 and Msn4. We find that Msn2 and Msn4 promote ATG8 expression downstream of the histone deacetylase complex (HDAC) subunit Ume6, a previously identified negative regulator of ATG8 expression. Moreover, we demonstrate that TORC2-Ypk1 signaling is functionally linked to distinct mitochondrial respiratory complexes. Surprisingly, we find that autophagy flux during amino acid starvation is also dependent upon Msn2-Msn4 activity, revealing a broad role for these transcription factors in the autophagy response.
MeSH term(s)	Amino Acids/deficiency ; Autophagy/genetics ; Autophagy-Related Protein 8 Family/genetics ; DNA-Binding Proteins/metabolism ; Gene Expression Regulation, Fungal ; Glycogen Synthase Kinase 3/metabolism ; Mechanistic Target of Rapamycin Complex 2/metabolism ; Mitochondria/metabolism ; Repressor Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Signal Transduction ; Stress, Physiological/genetics ; Transcription Factors/metabolism
Chemical Substances	ATG8 protein, S cerevisiae ; Amino Acids ; Autophagy-Related Protein 8 Family ; DNA-Binding Proteins ; MSN2 protein, S cerevisiae ; MSN4 protein, S cerevisiae ; Repressor Proteins ; Saccharomyces cerevisiae Proteins ; Transcription Factors ; UME6 protein, S cerevisiae ; Mechanistic Target of Rapamycin Complex 2 (EC 2.7.11.1) ; Glycogen Synthase Kinase 3 (EC 2.7.11.26) ; MCK1 protein, S cerevisiae (EC 2.7.12.1)
Language	English
Publishing date	2017-12-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2017.1356949
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